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Volumn 6, Issue 4, 2011, Pages

Directed evolution reveals the binding motif preference of the LC8/DYNLL hub protein and predicts large numbers of novel binders in the human proteome

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; BINDING PROTEIN; GLUTAMINE; LC8 DYNEIN LIGHT CHAIN; PROTEIN EML3; PROTEOME; UNCLASSIFIED DRUG; VALINE; CYTOPLASMIC DYNEIN; DNA; DYNLL1 PROTEIN, HUMAN;

EID: 79955142468     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0018818     Document Type: Article
Times cited : (56)

References (84)
  • 2
    • 38849199178 scopus 로고    scopus 로고
    • Dynein light chain LC8 is a dimerization hub essential in diverse protein networks
    • Barbar E, (2008) Dynein light chain LC8 is a dimerization hub essential in diverse protein networks. Biochemistry 47: 503-508.
    • (2008) Biochemistry , vol.47 , pp. 503-508
    • Barbar, E.1
  • 3
    • 77951297254 scopus 로고    scopus 로고
    • The LC8 family of dynein light chains: Multifunctional chaperon-like proteins
    • Hodi Z, Rapali P, Radnai L, Molnar T, Szenes A, et al. (2007) The LC8 family of dynein light chains: Multifunctional chaperon-like proteins. FEBS J 274: 106-106.
    • (2007) FEBS J , vol.274 , pp. 106
    • Hodi, Z.1    Rapali, P.2    Radnai, L.3    Molnar, T.4    Szenes, A.5
  • 4
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A, (1999) The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell 3: 287-296.
    • (1999) Mol Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 5
    • 0035823238 scopus 로고    scopus 로고
    • Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis
    • Puthalakath H, Villunger A, O'Reilly LA, Beaumont JG, Coultas L, et al. (2001) Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Science 293: 1829-1832.
    • (2001) Science , vol.293 , pp. 1829-1832
    • Puthalakath, H.1    Villunger, A.2    O'Reilly, L.A.3    Beaumont, J.G.4    Coultas, L.5
  • 6
    • 14844333111 scopus 로고    scopus 로고
    • The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation
    • Lo KW, Kan HM, Chan LN, Xu WG, Wang KP, et al. (2005) The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation. J Biol Chem 280: 8172-8179.
    • (2005) J Biol Chem , vol.280 , pp. 8172-8179
    • Lo, K.W.1    Kan, H.M.2    Chan, L.N.3    Xu, W.G.4    Wang, K.P.5
  • 7
    • 0034529440 scopus 로고    scopus 로고
    • Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila
    • Herzig RP, Andersson U, Scarpulla RC, (2000) Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila. J Cell Sci 113 (Pt 23): 4263-4273.
    • (2000) J Cell Sci , vol.113 , Issue.Pt 23 , pp. 4263-4273
    • Herzig, R.P.1    Andersson, U.2    Scarpulla, R.C.3
  • 8
    • 34347383511 scopus 로고    scopus 로고
    • Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex
    • Stelter P, Kunze R, Flemming D, Hopfner D, Diepholz M, et al. (2007) Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex. Nat Cell Biol 9: 788-796.
    • (2007) Nat Cell Biol , vol.9 , pp. 788-796
    • Stelter, P.1    Kunze, R.2    Flemming, D.3    Hopfner, D.4    Diepholz, M.5
  • 9
    • 67649464367 scopus 로고    scopus 로고
    • Interaction with LC8 is required for Pak1 nuclear import and is indispensable for zebrafish development
    • Lightcap CM, Kari G, Arias-Romero LE, Chernoff J, Rodeck U, et al. (2009) Interaction with LC8 is required for Pak1 nuclear import and is indispensable for zebrafish development. PLoS One 4: e6025.
    • (2009) PLoS One , vol.4
    • Lightcap, C.M.1    Kari, G.2    Arias-Romero, L.E.3    Chernoff, J.4    Rodeck, U.5
  • 10
    • 0033775766 scopus 로고    scopus 로고
    • Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein
    • Jacob Y, Badrane H, Ceccaldi PE, Tordo N, (2000) Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein. J Virol 74: 10217-10222.
    • (2000) J Virol , vol.74 , pp. 10217-10222
    • Jacob, Y.1    Badrane, H.2    Ceccaldi, P.E.3    Tordo, N.4
  • 11
    • 2942603255 scopus 로고    scopus 로고
    • Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes
    • Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, et al. (2004) Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes. Cancer Cell 5: 575-585.
    • (2004) Cancer Cell , vol.5 , pp. 575-585
    • Vadlamudi, R.K.1    Bagheri-Yarmand, R.2    Yang, Z.3    Balasenthil, S.4    Nguyen, D.5
  • 12
    • 65349109217 scopus 로고    scopus 로고
    • Dynein light chain regulates axonal trafficking and synaptic levels of Bassoon
    • Fejtova A, Davydova D, Bischof F, Lazarevic V, Altrock WD, et al. (2009) Dynein light chain regulates axonal trafficking and synaptic levels of Bassoon. J Cell Biol 185: 341-355.
    • (2009) J Cell Biol , vol.185 , pp. 341-355
    • Fejtova, A.1    Davydova, D.2    Bischof, F.3    Lazarevic, V.4    Altrock, W.D.5
  • 13
    • 0034660288 scopus 로고    scopus 로고
    • Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein
    • Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, et al. (2000) Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein. J Neurosci 20: 4524-4534.
    • (2000) J Neurosci , vol.20 , pp. 4524-4534
    • Naisbitt, S.1    Valtschanoff, J.2    Allison, D.W.3    Sala, C.4    Kim, E.5
  • 14
    • 33745831897 scopus 로고    scopus 로고
    • Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells
    • Rayala SK, den Hollander P, Manavathi B, Talukder AH, Song C, et al. (2006) Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells. J Biol Chem 281: 19092-19099.
    • (2006) J Biol Chem , vol.281 , pp. 19092-19099
    • Rayala, S.K.1    den Hollander, P.2    Manavathi, B.3    Talukder, A.H.4    Song, C.5
  • 15
    • 0029977560 scopus 로고    scopus 로고
    • Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster
    • Dick T, Ray K, Salz HK, Chia W, (1996) Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster. Mol Cell Biol 16: 1966-1977.
    • (1996) Mol Cell Biol , vol.16 , pp. 1966-1977
    • Dick, T.1    Ray, K.2    Salz, H.K.3    Chia, W.4
  • 16
    • 0037448540 scopus 로고    scopus 로고
    • Systematic functional analysis of the Caenorhabditis elegans genome using RNAi
    • Kamath RS, Fraser AG, Dong Y, Poulin G, Durbin R, et al. (2003) Systematic functional analysis of the Caenorhabditis elegans genome using RNAi. Nature 421: 231-237.
    • (2003) Nature , vol.421 , pp. 231-237
    • Kamath, R.S.1    Fraser, A.G.2    Dong, Y.3    Poulin, G.4    Durbin, R.5
  • 17
    • 0033661719 scopus 로고    scopus 로고
    • The light chain composition of chicken brain myosin-Va: calmodulin, myosin-II essential light chains, and 8-kDa dynein light chain/PIN
    • Espindola FS, Suter DM, Partata LB, Cao T, Wolenski JS, et al. (2000) The light chain composition of chicken brain myosin-Va: calmodulin, myosin-II essential light chains, and 8-kDa dynein light chain/PIN. Cell Motil Cytoskeleton 47: 269-281.
    • (2000) Cell Motil Cytoskeleton , vol.47 , pp. 269-281
    • Espindola, F.S.1    Suter, D.M.2    Partata, L.B.3    Cao, T.4    Wolenski, J.S.5
  • 18
    • 1242337339 scopus 로고    scopus 로고
    • Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands
    • Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, et al. (2004) Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands. Biochem J 377: 597-605.
    • (2004) Biochem J , vol.377 , pp. 597-605
    • Day, C.L.1    Puthalakath, H.2    Skea, G.3    Strasser, A.4    Barsukov, I.5
  • 19
    • 37549035938 scopus 로고    scopus 로고
    • Interaction of the DYNLT (TCTEX1/RP3) light chains and the intermediate chains reveals novel intersubunit regulation during assembly of the dynein complex
    • Lo KW, Kogoy JM, Rasoul BA, King SM, Pfister KK, (2007) Interaction of the DYNLT (TCTEX1/RP3) light chains and the intermediate chains reveals novel intersubunit regulation during assembly of the dynein complex. J Biol Chem 282: 36871-36878.
    • (2007) J Biol Chem , vol.282 , pp. 36871-36878
    • Lo, K.W.1    Kogoy, J.M.2    Rasoul, B.A.3    King, S.M.4    Pfister, K.K.5
  • 20
    • 78649646795 scopus 로고    scopus 로고
    • Affinity, avidity and kinetics of target sequence binding to LC8 dynein light chain isoforms
    • Radnai L, Rapali P, Hodi Z, Suveges D, Molnar T, et al. (2010) Affinity, avidity and kinetics of target sequence binding to LC8 dynein light chain isoforms. J Biol Chem.
    • (2010) J Biol Chem
    • Radnai, L.1    Rapali, P.2    Hodi, Z.3    Suveges, D.4    Molnar, T.5
  • 21
    • 0031791314 scopus 로고    scopus 로고
    • Solution structure of a protein inhibitor of neuronal nitric oxide synthase
    • Tochio H, Ohki S, Zhang Q, Li M, Zhang M, (1998) Solution structure of a protein inhibitor of neuronal nitric oxide synthase. Nat Struct Biol 5: 965-969.
    • (1998) Nat Struct Biol , vol.5 , pp. 965-969
    • Tochio, H.1    Ohki, S.2    Zhang, Q.3    Li, M.4    Zhang, M.5
  • 23
    • 0035830488 scopus 로고    scopus 로고
    • Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain
    • Fan J, Zhang Q, Tochio H, Li M, Zhang M, (2001) Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain. J Mol Biol 306: 97-108.
    • (2001) J Mol Biol , vol.306 , pp. 97-108
    • Fan, J.1    Zhang, Q.2    Tochio, H.3    Li, M.4    Zhang, M.5
  • 24
    • 34547144408 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex
    • Williams JC, Roulhac PL, Roy AG, Vallee RB, Fitzgerald MC, et al. (2007) Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex. Proc Natl Acad Sci U S A 104: 10028-10033.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 10028-10033
    • Williams, J.C.1    Roulhac, P.L.2    Roy, A.G.3    Vallee, R.B.4    Fitzgerald, M.C.5
  • 25
    • 34447277680 scopus 로고    scopus 로고
    • Structure and dynamics of LC8 complexes with KXTQT-motif peptides: swallow and dynein intermediate chain compete for a common site
    • Benison G, Karplus PA, Barbar E, (2007) Structure and dynamics of LC8 complexes with KXTQT-motif peptides: swallow and dynein intermediate chain compete for a common site. J Mol Biol 371: 457-468.
    • (2007) J Mol Biol , vol.371 , pp. 457-468
    • Benison, G.1    Karplus, P.A.2    Barbar, E.3
  • 26
    • 56249132454 scopus 로고    scopus 로고
    • The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8
    • Benison G, Karplus PA, Barbar E, (2008) The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8. J Mol Biol 384: 954-966.
    • (2008) J Mol Biol , vol.384 , pp. 954-966
    • Benison, G.1    Karplus, P.A.2    Barbar, E.3
  • 27
    • 0142039800 scopus 로고    scopus 로고
    • Structure of the monomeric 8-kDa dynein light chain and mechanism of the domain-swapped dimer assembly
    • Wang W, Lo KW, Kan HM, Fan JS, Zhang M, (2003) Structure of the monomeric 8-kDa dynein light chain and mechanism of the domain-swapped dimer assembly. J Biol Chem 278: 41491-41499.
    • (2003) J Biol Chem , vol.278 , pp. 41491-41499
    • Wang, W.1    Lo, K.W.2    Kan, H.M.3    Fan, J.S.4    Zhang, M.5
  • 29
    • 34250815165 scopus 로고    scopus 로고
    • Characterization of molecular recognition features, MoRFs, and their binding partners
    • Vacic V, Oldfield CJ, Mohan A, Radivojac P, Cortese MS, et al. (2007) Characterization of molecular recognition features, MoRFs, and their binding partners. J Proteome Res 6: 2351-2366.
    • (2007) J Proteome Res , vol.6 , pp. 2351-2366
    • Vacic, V.1    Oldfield, C.J.2    Mohan, A.3    Radivojac, P.4    Cortese, M.S.5
  • 30
    • 33750054653 scopus 로고    scopus 로고
    • Alternatively spliced exon B of myosin Va is essential for binding the tail-associated light chain shared by dynein
    • Hodi Z, Nemeth AL, Radnai L, Hetenyi C, Schlett K, et al. (2006) Alternatively spliced exon B of myosin Va is essential for binding the tail-associated light chain shared by dynein. Biochemistry 45: 12582-12595.
    • (2006) Biochemistry , vol.45 , pp. 12582-12595
    • Hodi, Z.1    Nemeth, A.L.2    Radnai, L.3    Hetenyi, C.4    Schlett, K.5
  • 31
    • 10644253619 scopus 로고    scopus 로고
    • The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8
    • Nyarko A, Hare M, Hays TS, Barbar E, (2004) The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8. Biochemistry 43: 15595-15603.
    • (2004) Biochemistry , vol.43 , pp. 15595-15603
    • Nyarko, A.1    Hare, M.2    Hays, T.S.3    Barbar, E.4
  • 32
    • 33749012287 scopus 로고    scopus 로고
    • The binding of DYNLL2 to myosin Va requires alternatively spliced exon B and stabilizes a portion of the myosin's coiled-coil domain
    • Wagner W, Fodor E, Ginsburg A, Hammer JA 3rd, (2006) The binding of DYNLL2 to myosin Va requires alternatively spliced exon B and stabilizes a portion of the myosin's coiled-coil domain. Biochemistry 45: 11564-11577.
    • (2006) Biochemistry , vol.45 , pp. 11564-11577
    • Wagner, W.1    Fodor, E.2    Ginsburg, A.3    Hammer 3rd, J.A.4
  • 33
    • 0035958082 scopus 로고    scopus 로고
    • The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif
    • Lo KW, Naisbitt S, Fan JS, Sheng M, Zhang M, (2001) The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif. J Biol Chem 276: 14059-14066.
    • (2001) J Biol Chem , vol.276 , pp. 14059-14066
    • Lo, K.W.1    Naisbitt, S.2    Fan, J.S.3    Sheng, M.4    Zhang, M.5
  • 34
    • 0035903004 scopus 로고    scopus 로고
    • Identification of novel cellular proteins that bind to the LC8 dynein light chain using a pepscan technique
    • Rodriguez-Crespo I, Yelamos B, Roncal F, Albar JP, Ortiz de Montellano PR, et al. (2001) Identification of novel cellular proteins that bind to the LC8 dynein light chain using a pepscan technique. FEBS Lett 503: 135-141.
    • (2001) FEBS Lett , vol.503 , pp. 135-141
    • Rodriguez-Crespo, I.1    Yelamos, B.2    Roncal, F.3    Albar, J.P.4    Ortiz de Montellano, P.R.5
  • 35
    • 55249119108 scopus 로고    scopus 로고
    • Biochemical and structural characterization of the Pak1-LC8 interaction
    • Lightcap CM, Sun S, Lear JD, Rodeck U, Polenova T, et al. (2008) Biochemical and structural characterization of the Pak1-LC8 interaction. J Biol Chem 283: 27314-27324.
    • (2008) J Biol Chem , vol.283 , pp. 27314-27324
    • Lightcap, C.M.1    Sun, S.2    Lear, J.D.3    Rodeck, U.4    Polenova, T.5
  • 36
    • 77951708885 scopus 로고    scopus 로고
    • Structural basis for the interaction between dynein light chain 1 and the glutamate channel homolog GRINL1A
    • Garcia-Mayoral MF, Martinez-Moreno M, Albar JP, Rodriguez-Crespo I, Bruix M, (2010) Structural basis for the interaction between dynein light chain 1 and the glutamate channel homolog GRINL1A. FEBS J 277: 2340-2350.
    • (2010) FEBS J , vol.277 , pp. 2340-2350
    • Garcia-Mayoral, M.F.1    Martinez-Moreno, M.2    Albar, J.P.3    Rodriguez-Crespo, I.4    Bruix, M.5
  • 37
    • 4043144340 scopus 로고    scopus 로고
    • Cellulose membrane supported peptide arrays for deciphering protein-protein interaction sites: the case of PIN, a protein with multiple natural partners
    • Lajoix AD, Gross R, Aknin C, Dietz S, Granier C, et al. (2004) Cellulose membrane supported peptide arrays for deciphering protein-protein interaction sites: the case of PIN, a protein with multiple natural partners. Mol Divers 8: 281-290.
    • (2004) Mol Divers , vol.8 , pp. 281-290
    • Lajoix, A.D.1    Gross, R.2    Aknin, C.3    Dietz, S.4    Granier, C.5
  • 38
    • 56249116551 scopus 로고    scopus 로고
    • Differences in dynamic structure of LC8 monomer, dimer, and dimer-peptide complexes
    • Hall J, Hall A, Pursifull N, Barbar E, (2008) Differences in dynamic structure of LC8 monomer, dimer, and dimer-peptide complexes. Biochemistry 47: 11940-11952.
    • (2008) Biochemistry , vol.47 , pp. 11940-11952
    • Hall, J.1    Hall, A.2    Pursifull, N.3    Barbar, E.4
  • 39
    • 42949104734 scopus 로고    scopus 로고
    • Serine 88 phosphorylation of the 8-kDa dynein light chain 1 is a molecular switch for its dimerization status and functions
    • Song C, Wen W, Rayala SK, Chen M, Ma J, et al. (2008) Serine 88 phosphorylation of the 8-kDa dynein light chain 1 is a molecular switch for its dimerization status and functions. J Biol Chem 283: 4004-4013.
    • (2008) J Biol Chem , vol.283 , pp. 4004-4013
    • Song, C.1    Wen, W.2    Rayala, S.K.3    Chen, M.4    Ma, J.5
  • 40
    • 10644221806 scopus 로고    scopus 로고
    • Dynein light chain LC8 promotes assembly of the coiled-coil domain of swallow protein
    • Wang L, Hare M, Hays TS, Barbar E, (2004) Dynein light chain LC8 promotes assembly of the coiled-coil domain of swallow protein. Biochemistry 43: 4611-4620.
    • (2004) Biochemistry , vol.43 , pp. 4611-4620
    • Wang, L.1    Hare, M.2    Hays, T.S.3    Barbar, E.4
  • 41
    • 0347634533 scopus 로고    scopus 로고
    • Bivalent antibody phage display mimics natural immunoglobulin
    • Lee CV, Sidhu SS, Fuh G, (2004) Bivalent antibody phage display mimics natural immunoglobulin. J Immunol Methods 284: 119-132.
    • (2004) J Immunol Methods , vol.284 , pp. 119-132
    • Lee, C.V.1    Sidhu, S.S.2    Fuh, G.3
  • 42
    • 0025259656 scopus 로고
    • The human growth hormone receptor. Secretion from Escherichia coli and disulfide bonding pattern of the extracellular binding domain
    • Fuh G, Mulkerrin MG, Bass S, McFarland N, Brochier M, et al. (1990) The human growth hormone receptor. Secretion from Escherichia coli and disulfide bonding pattern of the extracellular binding domain. J Biol Chem 265: 3111-3115.
    • (1990) J Biol Chem , vol.265 , pp. 3111-3115
    • Fuh, G.1    Mulkerrin, M.G.2    Bass, S.3    McFarland, N.4    Brochier, M.5
  • 43
    • 0033522202 scopus 로고    scopus 로고
    • A phagemid vector using the E. coli phage shock promoter facilitates phage display of toxic proteins
    • Beekwilder J, Rakonjac J, Jongsma M, Bosch D, (1999) A phagemid vector using the E. coli phage shock promoter facilitates phage display of toxic proteins. Gene 228: 23-31.
    • (1999) Gene , vol.228 , pp. 23-31
    • Beekwilder, J.1    Rakonjac, J.2    Jongsma, M.3    Bosch, D.4
  • 45
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: can low affinity systems be studied by isothermal titration calorimetry?
    • Turnbull WB, Daranas AH, (2003) On the value of c: can low affinity systems be studied by isothermal titration calorimetry? J Am Chem Soc 125: 14859-14866.
    • (2003) J Am Chem Soc , vol.125 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 46
    • 14744305626 scopus 로고    scopus 로고
    • Intramolecular cooperativity in a protein binding site assessed by combinatorial shotgun scanning mutagenesis
    • Pal G, Ultsch MH, Clark KP, Currell B, Kossiakoff AA, et al. (2005) Intramolecular cooperativity in a protein binding site assessed by combinatorial shotgun scanning mutagenesis. J Mol Biol 347: 489-494.
    • (2005) J Mol Biol , vol.347 , pp. 489-494
    • Pal, G.1    Ultsch, M.H.2    Clark, K.P.3    Currell, B.4    Kossiakoff, A.A.5
  • 47
    • 34249330325 scopus 로고    scopus 로고
    • When the surface tells what lies beneath: combinatorial phage-display mutagenesis reveals complex networks of surface-core interactions in the pacifastin protease inhibitor family
    • Szenthe B, Patthy A, Gaspari Z, Kekesi AK, Graf L, et al. (2007) When the surface tells what lies beneath: combinatorial phage-display mutagenesis reveals complex networks of surface-core interactions in the pacifastin protease inhibitor family. J Mol Biol 370: 63-79.
    • (2007) J Mol Biol , vol.370 , pp. 63-79
    • Szenthe, B.1    Patthy, A.2    Gaspari, Z.3    Kekesi, A.K.4    Graf, L.5
  • 48
    • 77958128617 scopus 로고    scopus 로고
    • Selective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin-associated serine protease (MASP)-1 and -2: significant contribution of MASP-1 to lectin pathway activation
    • Kocsis A, Kekesi KA, Szasz R, Vegh BM, Balczer J, et al. Selective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin-associated serine protease (MASP)-1 and-2: significant contribution of MASP-1 to lectin pathway activation. J Immunol 185: 4169-4178.
    • J Immunol , vol.185 , pp. 4169-4178
    • Kocsis, A.1    Kekesi, K.A.2    Szasz, R.3    Vegh, B.M.4    Balczer, J.5
  • 49
    • 33746799726 scopus 로고    scopus 로고
    • Comprehensive and quantitative mapping of energy landscapes for protein-protein interactions by rapid combinatorial scanning
    • Pal G, Kouadio JL, Artis DR, Kossiakoff AA, Sidhu SS, (2006) Comprehensive and quantitative mapping of energy landscapes for protein-protein interactions by rapid combinatorial scanning. J Biol Chem 281: 22378-22385.
    • (2006) J Biol Chem , vol.281 , pp. 22378-22385
    • Pal, G.1    Kouadio, J.L.2    Artis, D.R.3    Kossiakoff, A.A.4    Sidhu, S.S.5
  • 50
    • 0043237620 scopus 로고    scopus 로고
    • The functional binding epitope of a high affinity variant of human growth hormone mapped by shotgun alanine-scanning mutagenesis: insights into the mechanisms responsible for improved affinity
    • Pal G, Kossiakoff AA, Sidhu SS, (2003) The functional binding epitope of a high affinity variant of human growth hormone mapped by shotgun alanine-scanning mutagenesis: insights into the mechanisms responsible for improved affinity. J Mol Biol 332: 195-204.
    • (2003) J Mol Biol , vol.332 , pp. 195-204
    • Pal, G.1    Kossiakoff, A.A.2    Sidhu, S.S.3
  • 52
    • 46249092087 scopus 로고    scopus 로고
    • EML3 is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase
    • Tegha-Dunghu J, Neumann B, Reber S, Krause R, Erfle H, et al. (2008) EML3 is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. J Cell Sci 121: 1718-1726.
    • (2008) J Cell Sci , vol.121 , pp. 1718-1726
    • Tegha-Dunghu, J.1    Neumann, B.2    Reber, S.3    Krause, R.4    Erfle, H.5
  • 53
    • 0037415014 scopus 로고    scopus 로고
    • Exploring protein-protein interactions with phage display
    • Sidhu SS, Fairbrother WJ, Deshayes K, (2003) Exploring protein-protein interactions with phage display. Chembiochem 4: 14-25.
    • (2003) Chembiochem , vol.4 , pp. 14-25
    • Sidhu, S.S.1    Fairbrother, W.J.2    Deshayes, K.3
  • 54
    • 0032538882 scopus 로고    scopus 로고
    • Recognition specificity of individual EH domains of mammals and yeast
    • Paoluzi S, Castagnoli L, Lauro I, Salcini AE, Coda L, et al. (1998) Recognition specificity of individual EH domains of mammals and yeast. Embo J 17: 6541-6550.
    • (1998) Embo J , vol.17 , pp. 6541-6550
    • Paoluzi, S.1    Castagnoli, L.2    Lauro, I.3    Salcini, A.E.4    Coda, L.5
  • 55
    • 0034647505 scopus 로고    scopus 로고
    • Analysis of PDZ domain-ligand interactions using carboxyl-terminal phage display
    • Fuh G, Pisabarro MT, Li Y, Quan C, Lasky LA, et al. (2000) Analysis of PDZ domain-ligand interactions using carboxyl-terminal phage display. J Biol Chem 275: 21486-21491.
    • (2000) J Biol Chem , vol.275 , pp. 21486-21491
    • Fuh, G.1    Pisabarro, M.T.2    Li, Y.3    Quan, C.4    Lasky, L.A.5
  • 56
    • 0037066692 scopus 로고    scopus 로고
    • The Erbin PDZ domain binds with high affinity and specificity to the carboxyl termini of delta-catenin and ARVCF
    • Laura RP, Witt AS, Held HA, Gerstner R, Deshayes K, et al. (2002) The Erbin PDZ domain binds with high affinity and specificity to the carboxyl termini of delta-catenin and ARVCF. J Biol Chem 277: 12906-12914.
    • (2002) J Biol Chem , vol.277 , pp. 12906-12914
    • Laura, R.P.1    Witt, A.S.2    Held, H.A.3    Gerstner, R.4    Deshayes, K.5
  • 57
    • 33746819780 scopus 로고    scopus 로고
    • Convergent and divergent ligand specificity among PDZ domains of the LAP and zonula occludens (ZO) families
    • Zhang Y, Yeh S, Appleton BA, Held HA, Kausalya PJ, et al. (2006) Convergent and divergent ligand specificity among PDZ domains of the LAP and zonula occludens (ZO) families. J Biol Chem 281: 22299-22311.
    • (2006) J Biol Chem , vol.281 , pp. 22299-22311
    • Zhang, Y.1    Yeh, S.2    Appleton, B.A.3    Held, H.A.4    Kausalya, P.J.5
  • 58
    • 34547559252 scopus 로고    scopus 로고
    • Structural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domain
    • Zhang Y, Appleton BA, Wu P, Wiesmann C, Sidhu SS, (2007) Structural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domain. Protein Sci 16: 1738-1750.
    • (2007) Protein Sci , vol.16 , pp. 1738-1750
    • Zhang, Y.1    Appleton, B.A.2    Wu, P.3    Wiesmann, C.4    Sidhu, S.S.5
  • 59
    • 34250748507 scopus 로고    scopus 로고
    • Identifying specificity profiles for peptide recognition modules from phage-displayed peptide libraries
    • Tonikian R, Zhang Y, Boone C, Sidhu SS, (2007) Identifying specificity profiles for peptide recognition modules from phage-displayed peptide libraries. Nat Protoc 2: 1368-1386.
    • (2007) Nat Protoc , vol.2 , pp. 1368-1386
    • Tonikian, R.1    Zhang, Y.2    Boone, C.3    Sidhu, S.S.4
  • 61
    • 0031588018 scopus 로고    scopus 로고
    • Modified phage peptide libraries as a tool to study specificity of phosphorylation and recognition of tyrosine containing peptides
    • Dente L, Vetriani C, Zucconi A, Pelicci G, Lanfrancone L, et al. (1997) Modified phage peptide libraries as a tool to study specificity of phosphorylation and recognition of tyrosine containing peptides. J Mol Biol 269: 694-703.
    • (1997) J Mol Biol , vol.269 , pp. 694-703
    • Dente, L.1    Vetriani, C.2    Zucconi, A.3    Pelicci, G.4    Lanfrancone, L.5
  • 62
    • 0029589911 scopus 로고
    • Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands
    • Feng S, Kasahara C, Rickles RJ, Schreiber SL, (1995) Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands. Proc Natl Acad Sci U S A 92: 12408-12415.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 12408-12415
    • Feng, S.1    Kasahara, C.2    Rickles, R.J.3    Schreiber, S.L.4
  • 63
    • 0028811162 scopus 로고
    • Phage display selection of ligand residues important for Src homology 3 domain binding specificity
    • Rickles RJ, Botfield MC, Zhou XM, Henry PA, Brugge JS, et al. (1995) Phage display selection of ligand residues important for Src homology 3 domain binding specificity. Proc Natl Acad Sci U S A 92: 10909-10913.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 10909-10913
    • Rickles, R.J.1    Botfield, M.C.2    Zhou, X.M.3    Henry, P.A.4    Brugge, J.S.5
  • 64
    • 0029959928 scopus 로고    scopus 로고
    • Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2
    • Sparks AB, Rider JE, Hoffman NG, Fowlkes DM, Quillam LA, et al. (1996) Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2. Proc Natl Acad Sci U S A 93: 1540-1544.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 1540-1544
    • Sparks, A.B.1    Rider, J.E.2    Hoffman, N.G.3    Fowlkes, D.M.4    Quillam, L.A.5
  • 65
    • 0035071216 scopus 로고    scopus 로고
    • Characterizing Class I WW domains defines key specificity determinants and generates mutant domains with novel specificities
    • Kasanov J, Pirozzi G, Uveges AJ, Kay BK, (2001) Characterizing Class I WW domains defines key specificity determinants and generates mutant domains with novel specificities. Chem Biol 8: 231-241.
    • (2001) Chem Biol , vol.8 , pp. 231-241
    • Kasanov, J.1    Pirozzi, G.2    Uveges, A.J.3    Kay, B.K.4
  • 66
  • 67
    • 0034681299 scopus 로고    scopus 로고
    • High copy display of large proteins on phage for functional selections
    • Sidhu SS, Weiss GA, Wells JA, (2000) High copy display of large proteins on phage for functional selections. J Mol Biol 296: 487-495.
    • (2000) J Mol Biol , vol.296 , pp. 487-495
    • Sidhu, S.S.1    Weiss, G.A.2    Wells, J.A.3
  • 68
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel TA, (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc Natl Acad Sci U S A 82: 488-492.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 69
    • 0042808434 scopus 로고    scopus 로고
    • Visualization of an unstable coiled coil from the scallop myosin rod
    • Li Y, Brown JH, Reshetnikova L, Blazsek A, Farkas L, et al. (2003) Visualization of an unstable coiled coil from the scallop myosin rod. Nature 424: 341-345.
    • (2003) Nature , vol.424 , pp. 341-345
    • Li, Y.1    Brown, J.H.2    Reshetnikova, L.3    Blazsek, A.4    Farkas, L.5
  • 71
    • 0041316988 scopus 로고    scopus 로고
    • Novel class of bivalent glutathione S-transferase inhibitors
    • Lyon RP, Hill JJ, Atkins WM, (2003) Novel class of bivalent glutathione S-transferase inhibitors. Biochemistry 42: 10418-10428.
    • (2003) Biochemistry , vol.42 , pp. 10418-10428
    • Lyon, R.P.1    Hill, J.J.2    Atkins, W.M.3
  • 72
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W, (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 26: 795-800.
    • (1993) J Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 74
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project N
    • Collaborative Computational Project N (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 77
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 79
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn MIaGNM M, (2000) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Cryst 57: 122-133.
    • (2000) Acta Cryst , vol.57 , pp. 122-133
    • Winn MIaGNM, M.1
  • 81
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski RA, Moss DS, Thornton JM, (1993) Main-chain bond lengths and bond angles in protein structures. J Mol Biol 231: 1049-1067.
    • (1993) J Mol Biol , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 82
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010
    • UniProt T, (2010) The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res 38: D142-148.
    • (2010) Nucleic Acids Res , vol.38
    • UniProt, T.1
  • 83
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I, (2005) The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J Mol Biol 347: 827-839.
    • (2005) J Mol Biol , vol.347 , pp. 827-839
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 84
    • 77951295640 scopus 로고    scopus 로고
    • Folded-unfolded cross-predictions and protein evolution: the case study of coiled-coils
    • Szappanos B, Suveges D, Nyitray L, Perczel A, Gaspari Z, (2010) Folded-unfolded cross-predictions and protein evolution: the case study of coiled-coils. FEBS Lett 584: 1623-1627.
    • (2010) FEBS Lett , vol.584 , pp. 1623-1627
    • Szappanos, B.1    Suveges, D.2    Nyitray, L.3    Perczel, A.4    Gaspari, Z.5


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